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Journal ArticleDOI

Nitrogenase. VIII. Mössbauer and EPR spectroscopy. The MoFe protein component from Azotobacter vinelandii OP.

TLDR
The Mössbauer investigation reveals three other spectral components characteristic of iron nuclei in an environment of integer or zero electronic spin, i.e. they reside in complexes which are "EPR-silent".
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This article is published in Biochimica et Biophysica Acta.The article was published on 1975-07-21. It has received 147 citations till now. The article focuses on the topics: Electron paramagnetic resonance & Spectral line.

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Journal ArticleDOI

Isolation of an iron-molybdenum cofactor from nitrogenase

TL;DR: The FeMoCo might be used as a model for synthesizing catalysts for chemical nitrogen fixation and knowledge of the structure of this cofactor should be useful for understanding the role of molybdenum at the active site of nitrogenase, role of ligands close to moly bdenum in electron and proton transfer, and the catalytic mechanism of nitrogen fixation.
Journal ArticleDOI

Isolation of a new vanadium-containing nitrogenase from Azotobacter vinelandii.

TL;DR: A new nitrogenase from Azotobacter vinelandii has been isolated and shown to differ completely from conventional component 1, i.e., the MoFe protein, which can reduce dinitrogen, protons, and acetylene but is only able to utilize 10-15% of its electrons for the reduction of acetylene.
Journal ArticleDOI

New insights into structure-function relationships in nitrogenase: A 1.6 A resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein.

TL;DR: The structures of the protein and the iron-molybdenum cofactor (FeMoco) appear to be largely unaffected by the redox status, although the movement of Ser beta90 and a surface helix in the beta subunit may be of functional significance.
Journal ArticleDOI

Reduction of Substrates by Nitrogenases

TL;DR: Progress in understanding the reduction of a wide range of C-based substrates, including CO and CO2, is discussed, and remaining challenges in understanding nitrogenase substrate reduction are considered.
References
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Journal ArticleDOI

Determination of serum proteins by means of the biuret reaction.

TL;DR: An investigation of the biochemical changes following experimental liver injury felt the need of a simple, rapid, and accurate method for determining the protein fractions in small amounts of serum and began with Kingsley’s biuret procedure.
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A direct microdetermination for sulfide.

TL;DR: The incorporation of sulfide into methylene blue in the presence of acidic N,N-dimethyl-p-phenylenediamine and ferric chloride has been utilized to provide a direct determination for sulfide at concentrations of 2 to 80 mμmoles per milliliter.
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Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins.

TL;DR: Nitrogenase from the facultative anaerobe Klebsiella pneumoniae was resolved into two protein components resembling those obtained from other nitrogen-fixing bacteria, both purified to homogeneity as shown by the criteria of disc electrophoresis and ultracentrifugal analysis.
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Micro methods for the quantitative determination of iron and copper in biological material.

TL;DR: This chapter describes the micro methods for the quantitative determination of iron and copper in biological material with essential features of wet ashing, evaporation of excess acid, reduction, neutralization with excess sodium acetate, development of color with a suitable bathophenanthroline, and extraction with a small quantity of organic solvent followed by spectrophotometric determination.
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Mössbauer spectroscopy of haem proteins.

TL;DR: From the physicist's point of view it appears reasonable to expect that the search for better agreement between theory and paramagnetic spectra may be a route to a better understanding of the factors affecting the quadrupole interaction.
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